메뉴 건너뛰기




Volumn 117, Issue , 2015, Pages 63-71

Intermolecular recognition of the non-coding RNA 7SK and HEXIM protein in perspective

Author keywords

HEXIM; Molecular interaction; Native mass spectrometry; non coding RNA 7SK; Transcription regulation

Indexed keywords

HEXIM PROTEIN; MONOMER; PROTEIN; UNCLASSIFIED DRUG; UNTRANSLATED RNA; 7SK METHYLPHOSPHATE CAPPING ENZYME, HUMAN; HEXIM1 PROTEIN, HUMAN; LARP7 PROTEIN, HUMAN; METHYLTRANSFERASE; PROTEIN BINDING; RIBONUCLEOPROTEIN; RNA BINDING PROTEIN;

EID: 84941600547     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2015.03.020     Document Type: Article
Times cited : (17)

References (55)
  • 1
    • 66449089824 scopus 로고    scopus 로고
    • 7SK RNA, a non-coding RNA regulating P-TEFb, a general transcription factor
    • G. Diribarne, and O. Bensaude 7SK RNA, a non-coding RNA regulating P-TEFb, a general transcription factor RNA Biol. 6 2009 122 128
    • (2009) RNA Biol. , vol.6 , pp. 122-128
    • Diribarne, G.1    Bensaude, O.2
  • 2
    • 0029011873 scopus 로고
    • Purification of P-TEFb, a transcription factor required for the transition into productive elongation
    • N.F. Marshall, and D.H. Price Purification of P-TEFb, a transcription factor required for the transition into productive elongation J. Biol. Chem. 270 1995 12335 12338
    • (1995) J. Biol. Chem. , vol.270 , pp. 12335-12338
    • Marshall, N.F.1    Price, D.H.2
  • 3
    • 33746403681 scopus 로고    scopus 로고
    • Controlling the elongation phase of transcription with P-TEFb
    • B.M. Peterlin, and D.H. Price Controlling the elongation phase of transcription with P-TEFb Mol. Cell 23 2006 297 305
    • (2006) Mol. Cell , vol.23 , pp. 297-305
    • Peterlin, B.M.1    Price, D.H.2
  • 4
    • 84889026690 scopus 로고    scopus 로고
    • RNA polymerase II transcription elongation control
    • J. Guo, and D.H. Price RNA polymerase II transcription elongation control Chem. Rev. 113 2013 8583 8603
    • (2013) Chem. Rev. , vol.113 , pp. 8583-8603
    • Guo, J.1    Price, D.H.2
  • 5
    • 84876842759 scopus 로고    scopus 로고
    • Signaling pathways differentially affect RNA polymerase II initiation, pausing, and elongation rate in cells
    • C.G. Danko, N. Hah, X. Luo, A.L. Martins, L. Core, J.T. Lis, A. Siepel, and W.L. Kraus Signaling pathways differentially affect RNA polymerase II initiation, pausing, and elongation rate in cells Mol. Cell 50 2013 212 222
    • (2013) Mol. Cell , vol.50 , pp. 212-222
    • Danko, C.G.1    Hah, N.2    Luo, X.3    Martins, A.L.4    Core, L.5    Lis, J.T.6    Siepel, A.7    Kraus, W.L.8
  • 6
    • 0031846856 scopus 로고    scopus 로고
    • The ability of positive transcription elongation factor B to transactivate human immunodeficiency virus transcription depends on a functional kinase domain, cyclin T1, and Tat
    • K. Fujinaga, T.P. Cujec, J. Peng, J. Garriga, D.H. Price, X. Grana, and B.M. Peterlin The ability of positive transcription elongation factor B to transactivate human immunodeficiency virus transcription depends on a functional kinase domain, cyclin T1, and Tat J. Virol. 72 1998 7154 7159
    • (1998) J. Virol. , vol.72 , pp. 7154-7159
    • Fujinaga, K.1    Cujec, T.P.2    Peng, J.3    Garriga, J.4    Price, D.H.5    Grana, X.6    Peterlin, B.M.7
  • 7
    • 0032701796 scopus 로고    scopus 로고
    • Tackling Tat
    • J. Karn Tackling Tat J. Mol. Biol. 293 1999 235 254
    • (1999) J. Mol. Biol. , vol.293 , pp. 235-254
    • Karn, J.1
  • 9
    • 34447321025 scopus 로고    scopus 로고
    • Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme
    • C. Jeronimo, D. Forget, A. Bouchard, Q. Li, G. Chua, C. Poitras, C. Therien, D. Bergeron, S. Bourassa, J. Greenblatt, and et al. Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme Mol. Cell 27 2007 262 274
    • (2007) Mol. Cell , vol.27 , pp. 262-274
    • Jeronimo, C.1    Forget, D.2    Bouchard, A.3    Li, Q.4    Chua, G.5    Poitras, C.6    Therien, C.7    Bergeron, D.8    Bourassa, S.9    Greenblatt, J.10
  • 10
    • 44649135099 scopus 로고    scopus 로고
    • The La-related protein LARP7 is a component of the 7SK ribonucleoprotein and affects transcription of cellular and viral polymerase II genes
    • A. Markert, M. Grimm, J. Martinez, J. Wiesner, A. Meyerhans, O. Meyuhas, A. Sickmann, and U. Fischer The La-related protein LARP7 is a component of the 7SK ribonucleoprotein and affects transcription of cellular and viral polymerase II genes EMBO Rep. 9 2008 569 575
    • (2008) EMBO Rep. , vol.9 , pp. 569-575
    • Markert, A.1    Grimm, M.2    Martinez, J.3    Wiesner, J.4    Meyerhans, A.5    Meyuhas, O.6    Sickmann, A.7    Fischer, U.8
  • 12
    • 40649100262 scopus 로고    scopus 로고
    • A La-related protein modulates 7SK snRNP integrity to suppress P-TEFb-dependent transcriptional elongation and tumorigenesis
    • N. He, N.S. Jahchan, E. Hong, Q. Li, M.A. Bayfield, R.J. Maraia, K. Luo, and Q. Zhou A La-related protein modulates 7SK snRNP integrity to suppress P-TEFb-dependent transcriptional elongation and tumorigenesis Mol. Cell 29 2008 588 599
    • (2008) Mol. Cell , vol.29 , pp. 588-599
    • He, N.1    Jahchan, N.S.2    Hong, E.3    Li, Q.4    Bayfield, M.A.5    Maraia, R.J.6    Luo, K.7    Zhou, Q.8
  • 13
    • 77449119756 scopus 로고    scopus 로고
    • A capping-independent function of MePCE in stabilizing 7SK snRNA and facilitating the assembly of 7SK snRNP
    • Y. Xue, Z. Yang, R. Chen, and Q. Zhou A capping-independent function of MePCE in stabilizing 7SK snRNA and facilitating the assembly of 7SK snRNP Nucleic Acids Res. 38 2010 360 369
    • (2010) Nucleic Acids Res. , vol.38 , pp. 360-369
    • Xue, Y.1    Yang, Z.2    Chen, R.3    Zhou, Q.4
  • 14
    • 84877291127 scopus 로고    scopus 로고
    • RNA elements directing in vivo assembly of the 7SK/MePCE/Larp7 transcriptional regulatory snRNP
    • L. Muniz, S. Egloff, and T. Kiss RNA elements directing in vivo assembly of the 7SK/MePCE/Larp7 transcriptional regulatory snRNP Nucleic Acids Res. 41 2013 4686 4698
    • (2013) Nucleic Acids Res. , vol.41 , pp. 4686-4698
    • Muniz, L.1    Egloff, S.2    Kiss, T.3
  • 15
    • 84905406642 scopus 로고    scopus 로고
    • Genetic analysis of the structure and function of 7SK small nuclear ribonucleoprotein (snRNP) in cells
    • K. Fujinaga, Z. Luo, and B.M. Peterlin Genetic analysis of the structure and function of 7SK small nuclear ribonucleoprotein (snRNP) in cells J. Biol. Chem. 289 2014 21181 21190
    • (2014) J. Biol. Chem. , vol.289 , pp. 21181-21190
    • Fujinaga, K.1    Luo, Z.2    Peterlin, B.M.3
  • 16
    • 0035891271 scopus 로고    scopus 로고
    • The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription
    • Z. Yang, Q. Zhu, K. Luo, and Q. Zhou The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription Nature 414 2001 317 322
    • (2001) Nature , vol.414 , pp. 317-322
    • Yang, Z.1    Zhu, Q.2    Luo, K.3    Zhou, Q.4
  • 17
    • 0035891288 scopus 로고    scopus 로고
    • 7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes
    • V.T. Nguyen, T. Kiss, A.A. Michels, and O. Bensaude 7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes Nature 414 2001 322 325
    • (2001) Nature , vol.414 , pp. 322-325
    • Nguyen, V.T.1    Kiss, T.2    Michels, A.A.3    Bensaude, O.4
  • 20
    • 29244474416 scopus 로고    scopus 로고
    • Interplay between 7SK snRNA and oppositely charged regions in HEXIM1 direct the inhibition of P-TEFb
    • M. Barboric, J. Kohoutek, J.P. Price, D. Blazek, D.H. Price, and B.M. Peterlin Interplay between 7SK snRNA and oppositely charged regions in HEXIM1 direct the inhibition of P-TEFb EMBO J. 24 2005 4291 4303
    • (2005) EMBO J. , vol.24 , pp. 4291-4303
    • Barboric, M.1    Kohoutek, J.2    Price, J.P.3    Blazek, D.4    Price, D.H.5    Peterlin, B.M.6
  • 21
    • 21644468867 scopus 로고    scopus 로고
    • Identification of a cyclin T-binding domain in Hexim1 and biochemical analysis of its binding competition with HIV-1 Tat
    • A. Schulte, N. Czudnochowski, M. Barboric, A. Schonichen, D. Blazek, B.M. Peterlin, and M. Geyer Identification of a cyclin T-binding domain in Hexim1 and biochemical analysis of its binding competition with HIV-1 Tat J. Biol. Chem. 280 2005 24968 24977
    • (2005) J. Biol. Chem. , vol.280 , pp. 24968-24977
    • Schulte, A.1    Czudnochowski, N.2    Barboric, M.3    Schonichen, A.4    Blazek, D.5    Peterlin, B.M.6    Geyer, M.7
  • 24
    • 78449234720 scopus 로고    scopus 로고
    • Controlling cellular P-TEFb activity by the HIV-1 transcriptional transactivator Tat
    • L. Muniz, S. Egloff, B. Ughy, B.E. Jady, and T. Kiss Controlling cellular P-TEFb activity by the HIV-1 transcriptional transactivator Tat PLoS Pathog. 6 2010 e1001152
    • (2010) PLoS Pathog. , vol.6 , pp. e1001152
    • Muniz, L.1    Egloff, S.2    Ughy, B.3    Jady, B.E.4    Kiss, T.5
  • 25
    • 84877975516 scopus 로고    scopus 로고
    • Extensive polymerase pausing during Drosophila axis patterning enables high-level and pliable transcription
    • A. Saunders, L.J. Core, C. Sutcliffe, J.T. Lis, and H.L. Ashe Extensive polymerase pausing during Drosophila axis patterning enables high-level and pliable transcription Genes Dev. 27 2013 1146 1158
    • (2013) Genes Dev. , vol.27 , pp. 1146-1158
    • Saunders, A.1    Core, L.J.2    Sutcliffe, C.3    Lis, J.T.4    Ashe, H.L.5
  • 27
    • 0025831431 scopus 로고
    • Structural analyses of the 7SK ribonucleoprotein (RNP), the most abundant human small RNP of unknown function
    • D.A. Wassarman, and J.A. Steitz Structural analyses of the 7SK ribonucleoprotein (RNP), the most abundant human small RNP of unknown function Mol. Cell. Biol. 11 1991 3432 3445
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3432-3445
    • Wassarman, D.A.1    Steitz, J.A.2
  • 31
    • 30644478471 scopus 로고    scopus 로고
    • Regulation of polymerase II transcription by 7SK snRNA: Two distinct RNA elements direct P-TEFb and HEXIM1 binding
    • S. Egloff, E. Van Herreweghe, and T. Kiss Regulation of polymerase II transcription by 7SK snRNA: two distinct RNA elements direct P-TEFb and HEXIM1 binding Mol. Cell. Biol. 26 2006 630 642
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 630-642
    • Egloff, S.1    Van Herreweghe, E.2    Kiss, T.3
  • 32
    • 60149099708 scopus 로고    scopus 로고
    • U30 of 7SK RNA forms a specific photo-cross-link with Hexim1 in the context of both a minimal RNA-binding site and a fully reconstituted 7SK/Hexim1/P-TEFb ribonucleoprotein complex
    • F. Belanger, H. Baigude, and T.M. Rana U30 of 7SK RNA forms a specific photo-cross-link with Hexim1 in the context of both a minimal RNA-binding site and a fully reconstituted 7SK/Hexim1/P-TEFb ribonucleoprotein complex J. Mol. Biol. 386 2009 1094 1107
    • (2009) J. Mol. Biol. , vol.386 , pp. 1094-1107
    • Belanger, F.1    Baigude, H.2    Rana, T.M.3
  • 33
    • 78649888513 scopus 로고    scopus 로고
    • HEXIM1 targets a repeated GAUC motif in the riboregulator of transcription 7SK and promotes base pair rearrangements
    • I. Lebars, D. Martinez-Zapien, A. Durand, J. Coutant, B. Kieffer, and A.C. Dock-Bregeon HEXIM1 targets a repeated GAUC motif in the riboregulator of transcription 7SK and promotes base pair rearrangements Nucleic Acids Res. 38 2010 7749 7763
    • (2010) Nucleic Acids Res. , vol.38 , pp. 7749-7763
    • Lebars, I.1    Martinez-Zapien, D.2    Durand, A.3    Coutant, J.4    Kieffer, B.5    Dock-Bregeon, A.C.6
  • 36
    • 34249053165 scopus 로고    scopus 로고
    • RNA-based affinity purification reveals 7SK RNPs with distinct composition and regulation
    • J.R. Hogg, and K. Collins RNA-based affinity purification reveals 7SK RNPs with distinct composition and regulation RNA 13 2007 868 880
    • (2007) RNA , vol.13 , pp. 868-880
    • Hogg, J.R.1    Collins, K.2
  • 38
    • 77957880315 scopus 로고    scopus 로고
    • The mechanism of release of P-TEFb and HEXIM1 from the 7SK snRNP by viral and cellular activators includes a conformational change in 7SK
    • B.J. Krueger, K. Varzavand, J.J. Cooper, and D.H. Price The mechanism of release of P-TEFb and HEXIM1 from the 7SK snRNP by viral and cellular activators includes a conformational change in 7SK PLoS One 5 2010 e12335
    • (2010) PLoS One , vol.5 , pp. e12335
    • Krueger, B.J.1    Varzavand, K.2    Cooper, J.J.3    Price, D.H.4
  • 39
    • 18144371989 scopus 로고    scopus 로고
    • HEXIM2, a HEXIM1-related protein, regulates positive transcription elongation factor b through association with 7SK
    • S.A. Byers, J.P. Price, J.J. Cooper, Q. Li, and D.H. Price HEXIM2, a HEXIM1-related protein, regulates positive transcription elongation factor b through association with 7SK J. Biol. Chem. 280 2005 16360 16367
    • (2005) J. Biol. Chem. , vol.280 , pp. 16360-16367
    • Byers, S.A.1    Price, J.P.2    Cooper, J.J.3    Li, Q.4    Price, D.H.5
  • 40
    • 0032419957 scopus 로고    scopus 로고
    • RNA recognition by arginine-rich peptide motifs
    • M.A. Weiss, and N. Narayana RNA recognition by arginine-rich peptide motifs Biopolymers 48 1998 167 180
    • (1998) Biopolymers , vol.48 , pp. 167-180
    • Weiss, M.A.1    Narayana, N.2
  • 41
    • 2942628287 scopus 로고    scopus 로고
    • A human immunodeficiency virus type 1 Tat-like arginine-rich RNA-binding domain is essential for HEXIM1 to inhibit RNA polymerase II transcription through 7SK snRNA-mediated inactivation of P-TEFb
    • J.H. Yik, R. Chen, A.C. Pezda, C.S. Samford, and Q. Zhou A human immunodeficiency virus type 1 Tat-like arginine-rich RNA-binding domain is essential for HEXIM1 to inhibit RNA polymerase II transcription through 7SK snRNA-mediated inactivation of P-TEFb Mol. Cell. Biol. 24 2004 5094 5105
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5094-5105
    • Yik, J.H.1    Chen, R.2    Pezda, A.C.3    Samford, C.S.4    Zhou, Q.5
  • 42
    • 84883034327 scopus 로고    scopus 로고
    • The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding
    • F. Casu, B.M. Duggan, and M. Hennig The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding Biophys. J. 105 2013 1004 1017
    • (2013) Biophys. J. , vol.105 , pp. 1004-1017
    • Casu, F.1    Duggan, B.M.2    Hennig, M.3
  • 44
    • 0032864043 scopus 로고    scopus 로고
    • Adaptive recognition in RNA complexes with peptides and protein modules
    • D.J. Patel Adaptive recognition in RNA complexes with peptides and protein modules Curr. Opin. Struct. Biol. 9 1999 74 87
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 74-87
    • Patel, D.J.1
  • 45
    • 0030475417 scopus 로고    scopus 로고
    • Deep penetration of an alpha-helix into a widened RNA major groove in the HIV-1 rev peptide-RNA aptamer complex
    • X. Ye, A. Gorin, A.D. Ellington, and D.J. Patel Deep penetration of an alpha-helix into a widened RNA major groove in the HIV-1 rev peptide-RNA aptamer complex Nat. Struct. Biol. 3 1996 1026 1033
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 1026-1033
    • Ye, X.1    Gorin, A.2    Ellington, A.D.3    Patel, D.J.4
  • 46
    • 24044525254 scopus 로고    scopus 로고
    • Transcription-dependent association of multiple positive transcription elongation factor units to a HEXIM multimer
    • C. Dulac, A.A. Michels, A. Fraldi, F. Bonnet, V.T. Nguyen, G. Napolitano, L. Lania, and O. Bensaude Transcription-dependent association of multiple positive transcription elongation factor units to a HEXIM multimer J. Biol. Chem. 280 2005 30619 30629
    • (2005) J. Biol. Chem. , vol.280 , pp. 30619-30629
    • Dulac, C.1    Michels, A.A.2    Fraldi, A.3    Bonnet, F.4    Nguyen, V.T.5    Napolitano, G.6    Lania, L.7    Bensaude, O.8
  • 47
    • 77950683267 scopus 로고    scopus 로고
    • A flexible bipartite coiled coil structure is required for the interaction of Hexim1 with the P-TEFB subunit cyclin T1
    • A. Schonichen, J.M. Bigalke, C. Urbanke, S. Grzesiek, S.A. Dames, and M. Geyer A flexible bipartite coiled coil structure is required for the interaction of Hexim1 with the P-TEFB subunit cyclin T1 Biochemistry 49 2010 3083 3091
    • (2010) Biochemistry , vol.49 , pp. 3083-3091
    • Schonichen, A.1    Bigalke, J.M.2    Urbanke, C.3    Grzesiek, S.4    Dames, S.A.5    Geyer, M.6
  • 49
    • 23344437022 scopus 로고    scopus 로고
    • Analysis of the large inactive P-TEFb complex indicates that it contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFb molecules containing Cdk9 phosphorylated at threonine 186
    • Q. Li, J.P. Price, S.A. Byers, D. Cheng, J. Peng, and D.H. Price Analysis of the large inactive P-TEFb complex indicates that it contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFb molecules containing Cdk9 phosphorylated at threonine 186 J. Biol. Chem. 280 2005 28819 28826
    • (2005) J. Biol. Chem. , vol.280 , pp. 28819-28826
    • Li, Q.1    Price, J.P.2    Byers, S.A.3    Cheng, D.4    Peng, J.5    Price, D.H.6
  • 50
    • 29244459405 scopus 로고    scopus 로고
    • Oligomerization of HEXIM1 via 7SK snRNA and coiled-coil region directs the inhibition of P-TEFb
    • D. Blazek, M. Barboric, J. Kohoutek, I. Oven, and B.M. Peterlin Oligomerization of HEXIM1 via 7SK snRNA and coiled-coil region directs the inhibition of P-TEFb Nucleic Acids Res. 33 2005 7000 7010
    • (2005) Nucleic Acids Res. , vol.33 , pp. 7000-7010
    • Blazek, D.1    Barboric, M.2    Kohoutek, J.3    Oven, I.4    Peterlin, B.M.5
  • 51
    • 34250377305 scopus 로고    scopus 로고
    • HEXIM1 is a promiscuous double-stranded RNA-binding protein and interacts with RNAs in addition to 7SK in cultured cells
    • Q. Li, J.J. Cooper, G.H. Altwerger, M.D. Feldkamp, M.A. Shea, and D.H. Price HEXIM1 is a promiscuous double-stranded RNA-binding protein and interacts with RNAs in addition to 7SK in cultured cells Nucleic Acids Res. 35 2007 2503 2512
    • (2007) Nucleic Acids Res. , vol.35 , pp. 2503-2512
    • Li, Q.1    Cooper, J.J.2    Altwerger, G.H.3    Feldkamp, M.D.4    Shea, M.A.5    Price, D.H.6
  • 52
    • 79959992840 scopus 로고    scopus 로고
    • Deciphering correct strategies for multiprotein complex assembly by co-expression: Application to complexes as large as the histone octamer
    • M.L. Diebold, S. Fribourg, M. Koch, T. Metzger, and C. Romier Deciphering correct strategies for multiprotein complex assembly by co-expression: application to complexes as large as the histone octamer J. Struct. Biol. 175 2011 178 188
    • (2011) J. Struct. Biol. , vol.175 , pp. 178-188
    • Diebold, M.L.1    Fribourg, S.2    Koch, M.3    Metzger, T.4    Romier, C.5
  • 53
    • 40449139010 scopus 로고    scopus 로고
    • The MC-Fold and MC-Sym pipeline infers RNA structure from sequence data
    • M. Parisien, and F. Major The MC-Fold and MC-Sym pipeline infers RNA structure from sequence data Nature 452 2008 51 55
    • (2008) Nature , vol.452 , pp. 51-55
    • Parisien, M.1    Major, F.2
  • 54
    • 0027049805 scopus 로고
    • The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: Crystal structure of the protein-DNA complex
    • T.E. Ellenberger, C.J. Brandl, K. Struhl, and S.C. Harrison The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex Cell 71 1992 1223 1237
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger, T.E.1    Brandl, C.J.2    Struhl, K.3    Harrison, S.C.4
  • 55
    • 0028894384 scopus 로고
    • Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA
    • J.N. Glover, and S.C. Harrison Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA Nature 373 1995 257 261
    • (1995) Nature , vol.373 , pp. 257-261
    • Glover, J.N.1    Harrison, S.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.